Polyamine oxidase activity in lymphoid tissues of glucocorticoid-treated rats

Ferioli, Maria Elena; Pinotti, Orietta; Pirona, Lorenza

doi:10.1016/s0006-2952(99)00280-4

Cited by 15 publications

(8 citation statements)

References 38 publications

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“…In the normal thymocytes used in the present investigation, the induction of apoptosis after etoposide treatment was paralleled by the decrease in total polyamine content and an increase in the activity of PAO which is consistent with previous observations suggesting a direct role of PAO in apoptosis induction [5,14]; our results also confirm that this enzyme is inducible also in thymocytes during apoptosis, as already shown by us [22,23,30] and others [4,14,40,41] for other cell systems, both in vivo and in vitro. Despite the lack of conclusive evidence about their role(s) in cell proliferation and apoptosis, polyamines have been taken as suitable targets for therapies which are specifically addressed to alter the cell cycle or induce cell death [3,5,7,19,20].…”

Section: Discussionsupporting

confidence: 93%

“…Aliquots of the supernatant were used to determine polyamine content by HPLC, as previously described [22]. Briefly, the polyamines were separated using a mBondapac C18 column and derivatized post-column by the O-phthalaldehyde method.…”

Section: Polyamine Analysismentioning

confidence: 99%

“…8]. In addition, our previous studies showed a positive correlation between PAO activity and apoptosis in rat thymus after hormonal treatments [22,23]. Mitoguazone (MGBG) is a guanidino-containing compound, structurally similar to spermidine, which exerts an inhibiting action on S-adenosylmethionine decarboxylase, i.e.…”

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confidence: 99%

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Administration of the antitumor drug mitoguazone protects normal thymocytes against spontaneous and etoposide-induced apoptosis

Ferioli¹,

Bottone

Soldani

et al. 2004

CMLS, Cell. Mol. Life Sci.

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The suggestion has been made that polyamines may be involved in the control of cell death, since exceedingly high or low levels induce apoptosis in different cell systems. For a deeper insight into the relationship between apoptosis and polyamine metabolism, we investigated in vitro the effect on rat thymocytes of mitoguazone (MGBG, which inhibits S-adenosylmethionine decarboxylase, i.e. a key enzyme in the polyamine biosynthetic pathway). Thymocytes were selected as an especially suitable model system, since they undergo spontaneous apoptosis in vivo and can be easily induced to apoptose in vitro by etoposide, used here as an apoptogenic agent. MGBG protected thymocytes from both spontaneous and drug-induced apoptosis, and this protective effect was associated with a decrease in polyamine oxidase activity and total polyamine levels.

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Section: Discussionsupporting

confidence: 93%

Section: Polyamine Analysismentioning

confidence: 99%

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Administration of the antitumor drug mitoguazone protects normal thymocytes against spontaneous and etoposide-induced apoptosis

Ferioli¹,

Bottone

Soldani

et al. 2004

CMLS, Cell. Mol. Life Sci.

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“…In addition to the very recent finding of Wang et al [11] that PAO is an enzyme inducible by certain polyamine analogues in the non-small-cell lung carcinoma cell line NCI H157, our study also demonstrates the inducibility of PAO in MCF-7 cells by other polyamine derivatives. Thus, the stimulation of PAO by anticancer polyamine analogues/derivatives extends knowledge on the inducibility of the enzyme shown by us [38,39] and others [40] in in vivo normal physiological models following hormonal treatment. While, however, PAO induction in polyamineanalogue-treated cancer cells might be involved in the mechanisms of cell death, enhanced PAO activity following hormonal treatment may play a role in supporting cell growth [38].…”

Section: Discussionsupporting

confidence: 57%

Biochemical effects and growth inhibition in MCF-7 cells caused by novel sulphonamido oxa-polyamine derivatives

Pavlov

Lin

Rodilla

2002

Cellular and Molecular Life Sciences (CMLS)

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The novel polyamine derivatives sulphonamido oxa-spermine (oxa-Spm) and sulphonamido oxa-spermidine (oxa-Spd) exhibited rapid cytotoxic action towards MCF-7 human breast cancer cells with IC50 values of 4.35 and 6.47 pM, respectively, after 24-h drug exposure. Neither compound is a substrate of serum amine oxidase. Both oxa-Spm and oxa-Spd caused cell shrinkage, as determined by phase-contrast microscopy. After incubation with 10 microM of either compound for 8 h, the cells underwent chromatin condensation and nuclear fragmentation. However, no clear DNA ladder was obtained by electrophoresis. The sulphonamido oxa-polyamine derivatives and especially oxa-Spd enhanced the activity of polyamine oxidase (PAO), an enzyme capable of oxidising N1-acetylated spermine and spermidine to spermidine and putrescine, respectively, generating cytotoxic H2O2 and 3-acetamidopropanal as by-products. The intracellular polyamine content was only marginally reduced in response to drug treatment. In conclusion, our data show that these novel sulphonamido oxa-polyamine derivatives possess high cytotoxic activity against MCF-7 cells and indicate that induction of PAO may mediate their cytotoxicity via apoptosis.

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“…1) Until several years ago, PAO was believed to be a constitutive enzyme with little is known about its physiological relevance. However, changes in PAO activity have been demonstrated in tissues during postnatal development or aging [4][5][6] and after treatment with certain drugs [7][8][9] or hormones, [10][11][12][13] confirming the inducibility of the enzyme. Recently, another polyamine catabolic enzyme was cloned as spermine oxidase (SMO) which oxidizes spermine (Spm) to Spd with H 2 O 2 production and is inducible when cells are treated with anticancer drugs.…”

mentioning

confidence: 98%

Assay of N1-Acetylpolyamine Oxidase Activity with N1,N11-Didansylnorspermine as the Substrate by Ion-Pair Reversed Phase High Performance Liquid Chromatography

Takao

Sugita

Shirahata

2010

Biological & Pharmaceutical Bulletin

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An assay method to measure N 1 -acetylpolyamine oxidase (PAO) activity with N 1 ,N 11 -didansylnorspermine (DiDNS333) as the substrate by high performance liquid chromatography (HPLC) was developed. Dansylpolyamines were synthesized, and their activity as a substrate for partially purified PAO from rat liver was evaluated. Among the dansylpolyamines, DiDNS333 was a useful substrate for the development of the PAO assay method. DiDNS333 was degraded by PAO to 1-dansylamido-3-propanal (DNS3al) and N 1 -dansylnorspermidine (DNS33). As DNS3al was separated into two peaks by HPLC of the assay mixture containing aminoguanidine, determination of DNS33 was used for the development of the assay method. When the assay method was applied to inhibition studies, the DNS33 peak on the chromatogram was consistently produced, and weak interference was found in the incubation with higher concentrations of natural polyamines. This result suggested that contaminating polyamines in biological samples do not interfere with this method. When the assay method was applied to cell extract from Chinese hamster ovary cell samples, the PAO activity, even at the low level in the cells, could easily be detected with as little as 10 mg of protein, which corresponds to 1؋10 5 cells. This HPLC method is a rapid, sensitive and useful assay for the measurement of PAO activity.

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Polyamine oxidase activity in lymphoid tissues of glucocorticoid-treated rats

Cited by 15 publications

References 38 publications

Administration of the antitumor drug mitoguazone protects normal thymocytes against spontaneous and etoposide-induced apoptosis

Administration of the antitumor drug mitoguazone protects normal thymocytes against spontaneous and etoposide-induced apoptosis

Biochemical effects and growth inhibition in MCF-7 cells caused by novel sulphonamido oxa-polyamine derivatives

Assay of N1-Acetylpolyamine Oxidase Activity with N1,N11-Didansylnorspermine as the Substrate by Ion-Pair Reversed Phase High Performance Liquid Chromatography

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